4CUK
Structure of Salmonella D-Lactate Dehydrogenase in complex with NADH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008720 | molecular_function | D-lactate dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008720 | molecular_function | D-lactate dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0051287 | molecular_function | NAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0008720 | molecular_function | D-lactate dehydrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0008720 | molecular_function | D-lactate dehydrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAI A 1331 |
| Chain | Residue |
| A | TYR100 |
| A | ASP174 |
| A | PRO175 |
| A | TYR176 |
| A | HIS204 |
| A | CYS205 |
| A | PRO206 |
| A | ASN211 |
| A | THR232 |
| A | SER233 |
| A | ASP258 |
| A | VAL105 |
| A | TYR260 |
| A | HIS295 |
| A | ALA297 |
| A | HOH2057 |
| A | HOH2075 |
| A | HOH2104 |
| A | ILE150 |
| A | GLY151 |
| A | THR152 |
| A | GLY153 |
| A | LYS154 |
| A | ILE155 |
| A | PHE173 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAI D 1331 |
| Chain | Residue |
| D | TYR100 |
| D | VAL105 |
| D | GLY151 |
| D | GLY153 |
| D | LYS154 |
| D | ILE155 |
| D | PHE173 |
| D | ASP174 |
| D | PRO175 |
| D | TYR176 |
| D | HIS204 |
| D | CYS205 |
| D | PRO206 |
| D | ASN211 |
| D | THR232 |
| D | SER233 |
| D | ASP258 |
| D | TYR260 |
| D | HIS295 |
| D | ALA297 |
| D | HOH2065 |
| D | HOH2086 |
Functional Information from PROSITE/UniProt
| site_id | PS00065 |
| Number of Residues | 28 |
| Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. AGVIGtGKIGvaalrilkgfgmr.LLaFD |
| Chain | Residue | Details |
| A | ALA147-ASP174 |
| site_id | PS00670 |
| Number of Residues | 23 |
| Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LFaeSDVIsLHcPltpeNyhLlN |
| Chain | Residue | Details |
| A | LEU194-ASN216 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKnGvMIINtSRGaLID |
| Chain | Residue | Details |
| A | MET223-ASP239 |
